SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A812

- RUVB_ECOLI

UniProt

P0A812 - RUVB_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Holliday junction ATP-dependent DNA helicase RuvB
Gene
ruvB, b1860, JW1849
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Enzyme regulationi

RuvB possesses weak ATPase activity, which is stimulated by the RuvA protein in the presence of DNA.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 698ATP Reviewed prediction

GO - Molecular functioni

  1. ATP bindingInferred from electronic annotationi Source: UniProtKB-HAMAP
  2. ATP-dependent DNA helicase activityInferred from direct assayi PubMed 8433990 Source: CACAO
  3. DNA bindingInferred from electronic annotationi Source: InterPro
  4. four-way junction helicase activityInferred from direct assayi PubMed 1608954PubMed 1617728 Source: EcoCyc
  5. protein bindingInferred from physical interactioni PubMed 21219465PubMed 9047358 Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. DNA duplex unwindingInferred from direct assayi PubMed 1608954PubMed 1617728PubMed 8433990 Source: GOC
  2. SOS responseInferred from expression patterni PubMed 2842314 Source: EcoCyc
  3. recombinational repairInferred from mutant phenotypei PubMed 6374379 Source: EcoCyc
  1. ATP-dependent DNA helicase activityInferred from direct assayi PubMed 8433990 Source: CACAO
  2. four-way junction helicase activityInferred from direct assayi PubMed 1608954PubMed 1617728 Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, SOS response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10924-MONOMER.
ECOL316407:JW1849-MONOMER.
MetaCyc:EG10924-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Holliday junction ATP-dependent DNA helicase RuvB (EC:3.6.4.12)
Gene namesi
Name:ruvB
Ordered Locus Names:b1860, JW1849
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10924. ruvB.

Subcellular locationi

Cytoplasm
Note: In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours.1 Publication

GO - Cellular componenti

  1. Holliday junction resolvase complexInferred from direct assayi PubMed 9160752 Source: EcoCyc
  2. cytoplasmInferred from electronic annotationi Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Holliday junction ATP-dependent DNA helicase RuvBUniRule annotation
PRO_0000165528Add
BLAST

Proteomic databases

PaxDbiP0A812.

Expressioni

Inductioni

Expression of the ruv region is induced by damage to DNA and is regulated by LexA as part of the SOS response. RuvA and RuvB are also involved in mutagenesis induced by UV and X irradiation and by some chemicals.2 Publications

Gene expression databases

GenevestigatoriP0A812.

Interactioni

Subunit structurei

Homododecamer composed of two hexameric rings; when bound to DNA in the presence of ATP and magnesium. Forms a complex with RuvA. Interacts with YgbT (Cas1).1 Publication

Protein-protein interaction databases

DIPiDIP-47870N.
IntActiP0A812. 15 interactions.
MINTiMINT-1266054.
STRINGi511145.b1860.

Structurei

3D structure databases

ProteinModelPortaliP0A812.
SMRiP0A812. Positions 22-333.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuvB family.

Phylogenomic databases

eggNOGiCOG2255.
HOGENOMiHOG000218623.
KOiK03551.
OMAiDYAEVKH.
OrthoDBiEOG6SR93S.
PhylomeDBiP0A812.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00016. DNA_helic_RuvB.
InterProiIPR003593. AAA+_ATPase.
IPR004605. DNA_helicase_Holl-junc_RuvB.
IPR008823. DNA_helicase_Holl-junc_RuvB_C.
IPR008824. DNA_helicase_Holl-junc_RuvB_N.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05491. RuvB_C. 1 hit.
PF05496. RuvB_N. 1 hit.
[Graphical view]
ProDomiPD005323. DNA_helicase_Holl-junc_RuvB_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00635. ruvB. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A812-1 [UniParc]FASTA

« Hide

MIEADRLISA GTTLPEDVAD RAIRPKLLEE YVGQPQVRSQ MEIFIKAAKL    50
RGDALDHLLI FGPPGLGKTT LANIVANEMG VNLRTTSGPV LEKAGDLAAM 100
LTNLEPHDVL FIDEIHRLSP VVEEVLYPAM EDYQLDIMIG EGPAARSIKI 150
DLPPFTLIGA TTRAGSLTSP LRDRFGIVQR LEFYQVPDLQ YIVSRSARFM 200
GLEMSDDGAL EVARRARGTP RIANRLLRRV RDFAEVKHDG TISADIAAQA 250
LDMLNVDAEG FDYMDRKLLL AVIDKFFGGP VGLDNLAAAI GEERETIEDV 300
LEPYLIQQGF LQRTPRGRMA TTRAWNHFGI TPPEMP 336
Length:336
Mass (Da):37,174
Last modified:August 1, 1988 - v1
Checksum:i79BAB4A9A5687F7C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07091 Genomic DNA. Translation: CAA30120.1.
M21298 Genomic DNA. Translation: AAA24613.1.
U00096 Genomic DNA. Translation: AAC74930.1.
AP009048 Genomic DNA. Translation: BAA15671.1.
PIRiBVECVB. B28533.
RefSeqiNP_416374.1. NC_000913.3.
YP_490122.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74930; AAC74930; b1860.
BAA15671; BAA15671; BAA15671.
GeneIDi12931888.
946371.
KEGGiecj:Y75_p1836.
eco:b1860.
PATRICi32119043. VBIEscCol129921_1939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07091 Genomic DNA. Translation: CAA30120.1 .
M21298 Genomic DNA. Translation: AAA24613.1 .
U00096 Genomic DNA. Translation: AAC74930.1 .
AP009048 Genomic DNA. Translation: BAA15671.1 .
PIRi BVECVB. B28533.
RefSeqi NP_416374.1. NC_000913.3.
YP_490122.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0A812.
SMRi P0A812. Positions 22-333.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-47870N.
IntActi P0A812. 15 interactions.
MINTi MINT-1266054.
STRINGi 511145.b1860.

Proteomic databases

PaxDbi P0A812.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74930 ; AAC74930 ; b1860 .
BAA15671 ; BAA15671 ; BAA15671 .
GeneIDi 12931888.
946371.
KEGGi ecj:Y75_p1836.
eco:b1860.
PATRICi 32119043. VBIEscCol129921_1939.

Organism-specific databases

EchoBASEi EB0917.
EcoGenei EG10924. ruvB.

Phylogenomic databases

eggNOGi COG2255.
HOGENOMi HOG000218623.
KOi K03551.
OMAi DYAEVKH.
OrthoDBi EOG6SR93S.
PhylomeDBi P0A812.

Enzyme and pathway databases

BioCyci EcoCyc:EG10924-MONOMER.
ECOL316407:JW1849-MONOMER.
MetaCyc:EG10924-MONOMER.

Miscellaneous databases

PROi P0A812.

Gene expression databases

Genevestigatori P0A812.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_00016. DNA_helic_RuvB.
InterProi IPR003593. AAA+_ATPase.
IPR004605. DNA_helicase_Holl-junc_RuvB.
IPR008823. DNA_helicase_Holl-junc_RuvB_C.
IPR008824. DNA_helicase_Holl-junc_RuvB_N.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF05491. RuvB_C. 1 hit.
PF05496. RuvB_N. 1 hit.
[Graphical view ]
ProDomi PD005323. DNA_helicase_Holl-junc_RuvB_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00635. ruvB. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequencing of the ruv region of Escherichia coli K-12 reveals a LexA regulated operon encoding two genes."
    Benson F.E., Illing G.T., Sharples G.J., Lloyd R.G.
    Nucleic Acids Res. 16:1541-1549(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: K12.
  2. "Structure and regulation of the Escherichia coli ruv operon involved in DNA repair and recombination."
    Shinagawa H., Makino K., Amemura M., Kimura S., Iwasaki H., Nakata A.
    J. Bacteriol. 170:4322-4329(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
    Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.
    , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
    DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro."
    Tsaneva I.R., Mueller B., West S.C.
    Proc. Natl. Acad. Sci. U.S.A. 90:1315-1319(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  7. "A dual function of the CRISPR-Cas system in bacterial antivirus immunity and DNA repair."
    Babu M., Beloglazova N., Flick R., Graham C., Skarina T., Nocek B., Gagarinova A., Pogoutse O., Brown G., Binkowski A., Phanse S., Joachimiak A., Koonin E.V., Savchenko A., Emili A., Greenblatt J., Edwards A.M., Yakunin A.F.
    Mol. Microbiol. 79:484-502(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YGBT, SUBCELLULAR LOCATION.
    Strain: K12.
  8. "Processing of recombination intermediates by the RuvABC proteins."
    West S.C.
    Annu. Rev. Genet. 31:213-244(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry nameiRUVB_ECOLI
AccessioniPrimary (citable) accession number: P0A812
Secondary accession number(s): P08577
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 11, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

External Data

Dasty 3

Similar proteinsi